About: Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis

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About: Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Deoxyribonucleoside regulator (DeoR) from Bacillus subtilis negatively regulates expression of enzymes involved in the catabolism of deoxyribonucleosides and deoxyribose. The DeoR protein is homologous to the sorbitol operon regulator family of metabolic regulators and comprises an N-terminal DNA-binding domain and a C-terminal effector-binding domain. We have determined the crystal structure of the effector-binding domain of DeoR (C-DeoR) in free form and in covalent complex with its effector deoxyribose-5-phosphate (dR5P). This is the first case of a covalently attached effector molecule captured in the structure of a bacterial transcriptional regulator. The dR5P molecule is attached through a Schiff base linkage to residue Lys141. The crucial role of Lys141 in effector binding was confirmed by mutational analysis and mass spectrometry of Schiff base adducts formed in solution. Structural analyses of the free and effector-bound C-DeoR structures provided a structural explanation for the mechanism of DeoR function as a molecular switch. Deoxyribonucleoside regulator (DeoR) from Bacillus subtilis negatively regulates expression of enzymes involved in the catabolism of deoxyribonucleosides and deoxyribose. The DeoR protein is homologous to the sorbitol operon regulator family of metabolic regulators and comprises an N-terminal DNA-binding domain and a C-terminal effector-binding domain. We have determined the crystal structure of the effector-binding domain of DeoR (C-DeoR) in free form and in covalent complex with its effector deoxyribose-5-phosphate (dR5P). This is the first case of a covalently attached effector molecule captured in the structure of a bacterial transcriptional regulator. The dR5P molecule is attached through a Schiff base linkage to residue Lys141. The crucial role of Lys141 in effector binding was confirmed by mutational analysis and mass spectrometry of Schiff base adducts formed in solution. Structural analyses of the free and effector-bound C-DeoR structures provided a structural explanation for the mechanism of DeoR function as a molecular switch. (en)
Title	Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis (en)
skos:prefLabel	Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis (en)
skos:notation	RIV/68378050:_____/14:00434086!RIV15-AV0-68378050
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(ME08016)
http://linked.open...iv/cisloPeriodika	18
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Fábry, Milan
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Ústav molekulární genetiky AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	47941
http://linked.open...ai/riv/idVysledku	RIV/68378050:_____/14:00434086
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	dimeric interface; effector binding; Schiff base; transcription repressor; X-ray crystallography (en)
http://linked.open.../riv/klicoveSlovo	X-ray crystallography Schiff base dimeric interface transcription repressor effector binding
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[062AC3655B97]
http://linked.open...i/riv/nazevZdroje	FEBS Journal
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Structural studies of transcriptional regulators of the DeoR and GntR families involved in catabolic repression in Bacillus subtilis.
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	281
http://linked.open...iv/tvurceVysledku	Fábry, Milan Hubálek, Martin Řezáčová, Pavlína Otwinowski, Z. Škerlová, Jana
http://linked.open...ain/vavai/riv/wos	000342584200023
issn	1742-464X
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.1111/febs.12856

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